Abstract.
Penicillin V acylase from Bacillus sphaericus was purified to homogeneity with an overall yield of 15%. The enzyme exhibited comparatively high specificity for penicillin V, penicillin G, and other related compounds being hydrolyzed at less than 10% of the rate of penicillin V. Moreover, the high rate of hydrolysis was observed when the side chain of the substrate molecule was unsubstituted. Lysine-modifying reagents inactivated the enzyme rapidly. Kinetics and titration studies indicated the involvement of lysine in the catalytic activity of the enzyme.
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Received: 10 July 1996 / Accepted: 26 August 1996
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Pundle, A., SivaRaman, H. Bacillus sphaericus Penicillin V Acylase: Purification, Substrate Specificity, and Active-Site Characterization . Curr Microbiol 34 , 144 –148 (1997). https://doi.org/10.1007/s002849900159
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DOI: https://doi.org/10.1007/s002849900159